ID L7LQ48_9ACTN Unreviewed; 201 AA.
AC L7LQ48;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Large ribosomal subunit protein bL25 {ECO:0000256|HAMAP-Rule:MF_01334};
DE AltName: Full=General stress protein CTC {ECO:0000256|HAMAP-Rule:MF_01334};
GN Name=rplY {ECO:0000256|HAMAP-Rule:MF_01334,
GN ECO:0000313|EMBL:GAC62292.1};
GN Synonyms=ctc {ECO:0000256|HAMAP-Rule:MF_01334};
GN ORFNames=GSI01S_32_00240 {ECO:0000313|EMBL:GAC62292.1};
OS Gordonia sihwensis NBRC 108236.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1223544 {ECO:0000313|EMBL:GAC62292.1, ECO:0000313|Proteomes:UP000035083};
RN [1] {ECO:0000313|EMBL:GAC62292.1, ECO:0000313|Proteomes:UP000035083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 108236 {ECO:0000313|EMBL:GAC62292.1,
RC ECO:0000313|Proteomes:UP000035083};
RA Yoshida I., Hosoyama A., Tsuchikane K., Ando Y., Baba S., Ohji S.,
RA Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia sihwensis NBRC 108236.";
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This is one of the proteins that binds to the 5S RNA in the
CC ribosome where it forms part of the central protuberance.
CC {ECO:0000256|HAMAP-Rule:MF_01334}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit; part of the 5S
CC rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA. Binds to the 5S rRNA
CC independently of L5 and L18. {ECO:0000256|HAMAP-Rule:MF_01334}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL25 family. CTC
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01334}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAC62292.1}.
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DR EMBL; BANU01000032; GAC62292.1; -; Genomic_DNA.
DR RefSeq; WP_006897698.1; NZ_BANU01000032.1.
DR AlphaFoldDB; L7LQ48; -.
DR eggNOG; COG1825; Bacteria.
DR Proteomes; UP000035083; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0008097; F:5S rRNA binding; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00495; Ribosomal_L25_TL5_CTC; 1.
DR Gene3D; 2.170.120.20; Ribosomal protein L25, beta domain; 1.
DR HAMAP; MF_01334; Ribosomal_L25_CTC; 1.
DR InterPro; IPR020056; Rbsml_bL25/Gln-tRNA_synth_N.
DR InterPro; IPR011035; Ribosomal_bL25/Gln-tRNA_synth.
DR InterPro; IPR020057; Ribosomal_bL25_b-dom.
DR InterPro; IPR037121; Ribosomal_bL25_C.
DR InterPro; IPR001021; Ribosomal_bL25_long.
DR InterPro; IPR029751; Ribosomal_L25_dom.
DR NCBIfam; TIGR00731; bL25_bact_ctc; 1.
DR PANTHER; PTHR33284; RIBOSOMAL PROTEIN L25/GLN-TRNA SYNTHETASE, ANTI-CODON-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR33284:SF1; RIBOSOMAL PROTEIN L25_GLN-TRNA SYNTHETASE, ANTI-CODON-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01386; Ribosomal_L25p; 1.
DR Pfam; PF14693; Ribosomal_TL5_C; 1.
DR SUPFAM; SSF50715; Ribosomal protein L25-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000035083};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01334};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01334};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01334};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW Rule:MF_01334}.
FT DOMAIN 7..93
FT /note="Large ribosomal subunit protein bL25 L25"
FT /evidence="ECO:0000259|Pfam:PF01386"
FT DOMAIN 101..180
FT /note="Large ribosomal subunit protein bL25 beta"
FT /evidence="ECO:0000259|Pfam:PF14693"
SQ SEQUENCE 201 AA; 21010 MW; F74437AC4F44DEAB CRC64;
MATAPQLAAA VREEKGKGAA RRARAAGQVP AVLYGHGTDP EHLLLPDREL AAILRANGVN
AVVELDIAGQ KQLALTKQVD VHPIRNYIEH VDLLIVKRGE KVNVEVAILI EGVAASGTLT
IQDASAVEVE AEALHIPENI VVDVHNLPAG TNVTAADLKL PAGVELITDP ETLVVTIEAA
KTAAETVGEE ADEEAAEDAA E
//
